title: [Regulation of thermal stability of enzymes by changing the composition of media. Native and modified alpha-chymotrypsin].
abstract: Stabilizing effect of denaturing salts on irreversible thermoinactivation of native and modified alpha-chymotrypsin at elevated temperatures is observed. The effect is caused by a shift of conformational equilibrium, at the primary step of reversible unfolding in the course of thermoinactivation, to a more unfolded form which is not able to refold "incorrectly". The stability of alpha-chymotrypsin is regulated within a wide range by medium alteration: the stabilizing effects are similar to those achieved by multipoint attachment of the enzyme to a support or by hydrophilization of protein by covalent modification.
authors.forename: V Iu
authors.initials: VIu
authors.lastname: Levitskiĭ
authors.forename: N S
authors.initials: NS
authors.lastname: Melik-Nubarov
authors.forename: V I
authors.initials: VI
authors.lastname: Slepnev
authors.forename: V A
authors.initials: VA
authors.lastname: Shikshnis
authors.forename: V V
authors.initials: VV
authors.lastname: Mozhaev
mesh_terms: D002918:Chymotrypsin / Q000378:metabolism*; D004795:Enzyme Stability; D006358:Hot Temperature; D011487:Protein Conformation; D011489:Protein Denaturation; D013050:Spectrometry, Fluorescence
chemical_list: D002918:Chymotrypsin
vernacular_title: Regulirovanie termostabil'nosti fermentov izmeneniem sostava sredy. Nativnyĭ i modifitsirovannyĭ alpha-khimotripsin.